title: Lytic enzyme produced by Pseudomonas aeruginosa concomitantly with bacteriophage PS17. Purification, characterization, and comparison with PR1-lysozyme.
abstract: A bacteriolytic enzyme was found to be produced, concomitantly with the progeny phage, in Pseudomonas aeruginosa P14 infected with phage PS17. The enzyme, named PS17-lysozyme, was purified by acrinol treatment, two cycles of Amberlite CG-50 chromatography, and SP-Sephadex C-50 chromatography. Homogeneity of the preparation was demonstrated by three electrophoretic techniques. PS17-lysozyme behaved like a basic protein (pI, 9-10) consisting of a single polypeptide chain (molecular weight, 24,500) and showed the substrate specificity as hen egg-white lysozyme. The enzyme exhibited much higher specific activity than the egg-white enzyme when assayed with chloroform-killed P. aeruginosa P14 as a substrate. These characteristics, as well as the amino acid composition, were very similar to those of PR1-lysozyme; a bacteriolytic enzyme produced in mitomycin C-induced P. aeruginosa P15 concomitantly with a phage-tail-like bacteriocin, pyocin R1 (Ochi et al. (1978) J. Biochem. 83, 727-736). However, the behavior of these two lysozymes from P. aeruginosa in Amberlite CG-50 chromatography and some other properties indicated that they were not identical, though they were similar. The results are in accord with the view that pyocin R1 may be a defective form of a bacteriophage closely related to but not identical with phage PS17.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D001435:Bacteriophages / Q000201:enzymology*; D004355:Drug Stability; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009113:Muramidase / Q000096:biosynthesis* / Q000302:isolation & purification; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D013045:Species Specificity; D013379:Substrate Specificity
chemical_list: D000596:Amino Acids; D009113:Muramidase